Several nmr experiments provide data which depend upon internuclear distances and details of molecular motion. An analysis of such information can provide useful insights into protein structures in solution and possibly will be applicable in studies of protein on membrane surfaces. It is intended to explore the use of fluorine nmr to elucidate protein structures from both experimental and theoretical directions; among the systems to be examined are examples involving small molecule-protein complexes, chemically modified proteins and proteins into which fluorinated amino acids have been incorporated biosynthetically.